ID   EFG_CHLMU               Reviewed;         694 AA.
AC   Q9PJV6;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Elongation factor G;
DE            Short=EF-G;
GN   Name=fusA; OrderedLocusNames=TC_0721;
OS   Chlamydia muridarum (strain MoPn / Nigg).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=243161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MoPn / Nigg;
RX   PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA   Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA   Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA   Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA   Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA   Salzberg S.L., Eisen J.A., Fraser C.M.;
RT   "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT   AR39.";
RL   Nucleic Acids Res. 28:1397-1406(2000).
CC   -!- FUNCTION: Catalyzes the GTP-dependent ribosomal translocation step
CC       during translation elongation. During this step, the ribosome changes
CC       from the pre-translocational (PRE) to the post-translocational (POST)
CC       state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound
CC       deacylated tRNA move to the P and E sites, respectively. Catalyzes the
CC       coordinated movement of the two tRNA molecules, the mRNA and
CC       conformational changes in the ribosome (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EF-G/EF-2
CC       subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE002160; AAF39532.1; -; Genomic_DNA.
DR   PIR; G81672; G81672.
DR   RefSeq; WP_010231341.1; NZ_CP027217.1.
DR   AlphaFoldDB; Q9PJV6; -.
DR   SMR; Q9PJV6; -.
DR   STRING; 243161.TC_0721; -.
DR   EnsemblBacteria; AAF39532; AAF39532; TC_0721.
DR   GeneID; 1246084; -.
DR   KEGG; cmu:TC_0721; -.
DR   eggNOG; COG0480; Bacteria.
DR   HOGENOM; CLU_002794_4_1_0; -.
DR   OMA; AATTCHW; -.
DR   OrthoDB; 88967at2; -.
DR   Proteomes; UP000000800; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR   CDD; cd16262; EFG_III; 1.
DR   CDD; cd01434; EFG_mtEFG1_IV; 1.
DR   CDD; cd03713; EFG_mtEFG_C; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00054_B; EF_G_EF_2_B; 1.
DR   InterPro; IPR041095; EFG_II.
DR   InterPro; IPR009022; EFG_III.
DR   InterPro; IPR035647; EFG_III/V.
DR   InterPro; IPR035649; EFG_V.
DR   InterPro; IPR000640; EFG_V-like.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR031157; G_TR_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR004540; Transl_elong_EFG/EF2.
DR   InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR   Pfam; PF00679; EFG_C; 1.
DR   Pfam; PF14492; EFG_III; 1.
DR   Pfam; PF03764; EFG_IV; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SMART; SM00838; EFG_C; 1.
DR   SMART; SM00889; EFG_IV; 1.
DR   SUPFAM; SSF50447; SSF50447; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF54980; SSF54980; 2.
DR   TIGRFAMs; TIGR00484; EF-G; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW   Protein biosynthesis.
FT   CHAIN           1..694
FT                   /note="Elongation factor G"
FT                   /id="PRO_0000091102"
FT   DOMAIN          9..288
FT                   /note="tr-type G"
FT   BINDING         18..25
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         82..86
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         136..139
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   694 AA;  76522 MW;  02A6B0E17DEA919D CRC64;
     MSDQEFGLDA IRNIGIMAHI DAGKTTTTER ILFYAGRTHK IGEVHEGGAT MDWMEQEQER
     GITITSAATT VFWLGSKINI IDTPGHVDFT IEVERSLRVL DGAVAVFDAV SGVEPQSETV
     WRQANKYGVP RVAFVNKMDR MGANYFGAVE SMREKLGANA IPVHCPIGAE SQFVGMVDLI
     SQKALYFLDD SLGAKWEERE IPEDLQEQCE VLRMQLLEEL ATVDETNEAF MEKVLEAPES
     ITEEEIHRVM RKGVIEGKIN PVLCGSAFKN KGVQQLLDVI VKWLPSPLDR GNVRGMNLKT
     GEEVCLKPSK DGPLAALAFK IMTDPYVGRI TFIRIYSGTL KKGSAILNST KDKKERISRL
     LEMHANERTD RDEFTVGDIG ACVGLKFSVT GDTLCDENQE IVLERIEAPE PVIDMAIEPK
     SKGDREKLAQ ALSALSEEDP TFRVSTNEET GQTIISGMGE LHLDILRDRM IREFKVEANV
     GKPQVSYKET ITKASDSETK YVKQSGGRGQ YAHVCLEIEP NEPGKGNEVV SKIVGGVIPK
     EYIPAVIKGV EEGLNSGVLA GYGLVDVKVS IVFGSYHEVD SSEMAFKICG SMAVKEACRK
     ALPVILEPIM KVTVITPEDH LGDVIGDLNR RRGKILGQEA SRNMAQVNAE VPLSEMFGYM
     TSLRSLTSGR ATSTMEPAFF AKVPQKIQEE IVKK